Cleavage of Arabidopsis PBS1 by a bacterial type III effector
Cleavage of Arabidopsis PBS1 by a bacterial type III effector
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DOI：
10.1126/science.1085671
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发表时间：
2003-08-29
期刊：
影响因子：
56.9
通讯作者：
Innes, RW
中科院分区：
文献类型：
--
作者：
Shao, F;Golstein, C;Innes, RW
植物抗病蛋白被认为是病原体无毒蛋白直接或间接产生的配体的受体。大多数Avr蛋白的生化功能是未知的，它们激活R蛋白的机制尚未确定。在拟南芥中，对表达AvrPphB的假单胞菌菌株的抗性需要RPS5和PBS 1，RPS5是具有预测的核苷酸结合位点和富含亮氨酸的重复序列的R蛋白类的成员，PBS 1是一种蛋白激酶。发现AvrPphB蛋白水解切割PBS 1，并且这种切割是RPS5介导的抗性所需的，这表明AvrPphB通过其酶活性间接检测。
Plant disease-resistance (R) proteins are thought to function as receptors for ligands produced directly or indirectly by pathogen avirulence (Avr) proteins. The biochemical functions of most Avr proteins are unknown, and the mechanisms by which they activate R proteins have not been determined. In Arabidopsis, resistance to Pseudomonas syringae strains expressing AvrPphB requires RPS5, a member of the class of R proteins that have a predicted nucleotide-binding site and leucine-rich repeats, and PBS1, a protein kinase. AvrPphB was found to proteolytically cleave PBS1, and this cleavage was required for RPS5-mediated resistance, which indicates that AvrPphB is detected indirectly via its enzymatic activity.